

Biochemistry for Life Sciences Exam Bank
Course Introduction
Biochemistry for Life Sciences explores the molecular foundations of biological processes, focusing on the chemical structure and function of biomolecules such as proteins, carbohydrates, lipids, and nucleic acids. The course covers essential metabolic pathways, enzyme kinetics, and regulatory mechanisms that enable living organisms to grow, reproduce, and adapt to their environments. Emphasis is placed on the application of biochemical principles to cellular processes, disease mechanisms, as well as laboratory techniques fundamental to modern life sciences research.
Recommended Textbook
Biochemistry 8th Edition by Jeremy M. Berg
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36 Chapters
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Page 2

Chapter 1: Biochemistry: An Evolving Science
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Sample Questions
Q1) The simplest way to depict stereochemistry is to use
A) ball-and-stick models.
B) ribbon diagrams.
C) space-filling models.
D) Fisher projections.
E) None of the answers is correct.
Answer: D
Q2) Provide a simple example of a process in which the entropy of a system changes. Answer: Several examples can be provided,including the random mixture of atoms when two different gases are mixed,or the creation of water molecules from energy gained following the mixture of oxygen and hydrogen under certain conditions.
Q3) What is the [A<sup>-</sup>]/[HA] ratio when a weak acid is in a solution one pH unit below its pK<sub>a</sub>?
A) 1:1
B) 1:10
C) 10:1
D) 2:1
E) None of the answers is correct.
Answer: B
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Chapter 2: Protein Composition and Structure
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Sample Questions
Q1) _____________________________ refers to the spatial arrangement of subunits and the nature of their interactions.
Answer: Quaternary structure
Q2) What is the charged group(s)present in glycine at a pH of 7?
A) -NH<sub>3</sub><sup>+</sup>
B) -COO<sup>-</sup>
C) -NH<sub>2</sub><sup>+</sup>
D) -NH<sub>3</sub><sup>+</sup> and -COO<sup>-</sup>
E) All the charged groups are present.
Answer: D
Q3) Collagen contains _____________________,a modified amino acid.
Answer: hydroxyproline
Q4) Which of the following amino acid residues would most likely be buried in the interior of a water-soluble,globular protein?
A) Asp
B) Ser
C) Phe
D) Lys
E) Gln
Answer: C

Page 4
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Chapter 3: Exploring Proteins and Proteomes
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Sample Questions
Q1) The unit for sedimentation coefficients is the _____.
A) Newton
B) radian
C) g
D) Svedberg
E) None of the answers is correct.
Answer: D
Q2) How can a protein's isoelectric point be used in protein purification (i.e.,isoelectric focusing)?
Answer: Isoelectric focusing is an electrophoretic technique in which a gradient charge is applied.Proteins migrate through the gradient field until they reach a point at which the pH is the same as the protein's pI.
Q3) Briefly describe how an ELISA works.
Answer: In ELISA,the antigen of interest is complexed with a specific antibody under appropriate assay conditions,and excess antibody is removed.The antibody is complexed to an enzyme,which can be measured quantitatively using an appropriate substrate and assay tool,often by a colorimetric product formation.
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Chapter 4: DNA, RNA, and the Flow of Genetic Information
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Sample Questions
Q1) What is the nucleotide sequence on the DNA template strand that yields the CUA codon for leucine?
A) AUC
B) TAG
C) CTA
D) GAT
E) CUA
Q2) What is the approximate error rate in DNA replication?
A) 1 *10S1U1P1-5S1S1P0S1S1P0
B) 1*10S1U1P1-5S1S1P0S1S1P0
C) 1 * 10S1U1P1-14S1S1P0
D) 1 * 10S1U1P1-11S1S1P0
E) None of the answers are correct.
Q3) The technique(s)used by Franklin and Wilkins to deduce the structure of DNA was A) absorbance spectrophotometry.
B) electron microscopy.
C) x-ray diffraction.
D) All of the answers are correct.
E) None of the answers is correct.
Q4) What is a consensus sequence?

Page 6
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Chapter 5: Exploring Genes and Genomes
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Q1) How is a gene gun used?
Q2) The Sanger technique for sequencing DNA involves the use of __________________ nucleotide analogs that terminate chain elongation.
Q3) What type of vector is used to produce large amounts of a desired protein in a bacterial cell?
A) cloning vector
B) replication vector
C) transcription vector
D) translation vector
E) expression vector
Q4) The specificity or stringency of a PCR reaction can be controlled by altering the reaction
A) volume.
B) target sequence.
C) temperature and salt concentration.
D) time.
E) None of the answers is correct.
Q5) If a gene is inserted into the gene that encodes an antibiotic resistance marker,will the resulting clone be sensitive or resistant to the antibiotic?
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Chapter 6: Exploring Evolution and Bioinformatics
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Q1) If a protein contains a repetitive region,what might be assumed,and what should be done next to test the hypothesis?
Q2) Why are protein comparisons of three-dimensional shape more revealing than primary sequences?
Q3) Analysis of substitution matrices indicates that cysteine (C)and __________________ residues tend to be conserved more than other amino acid residues.
Q4) An example of proteins that evolved similar mechanisms by convergent evolution is
A) DNA polymerase and elastase.
B) chymotrypsin and subtilisin.
C) neuramidase and glycolase.
D) actin and myosin.
E) None of the answers is correct.
Q5) How are three-dimensional structures useful in evolutionary comparisons?
Q6) What is a substitution matrix?
Q7) Briefly describe the ATP-RNA binding experiment showing that a structure had evolved that was capable of specific binding to ATP.
Q8) What are some of the inherent difficulties of using DNA from ancient samples?
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Chapter 7: Hemoglobin: a Portrait of a Protein in Action
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Q1) What is the composition of fetal hemoglobin?
A) two \(\alpha\) chains and two \(\beta\) chains.
B) two \(\alpha\) chains and two \(\gamma\) chains.
C) two \(\alpha\) chains and two \(\beta\) chains
D) two \(\alpha\) chains and two \(\delta\) chains
E) four \(\beta\) chains
Q2) What is neuroglobin,and what is its suspected role?
Q3) Describe the structure of normal adult hemoglobin.
Q4) What factor(s)influence(s)the binding of oxygen to myoglobin?
A) the concentration of bicarbonate ion, HCO<sub>3</sub><sup>-</sup>
B) the partial pressure of oxygen, pO<sub>2</sub>
C) the concentration of hemoglobin present
D) the concentration of 2,3-BPG
E) both the partial pressure of oxygen, pO<sub>2</sub>and the concentration of 2,3-BPG
Q5) As the partial pressure of carbon dioxide increases,the affinity of oxygen binding to hemoglobin ______________.
Q6) Describe how carbon dioxide affects the oxygenation of hemoglobin.
Q7) Under normal conditions,the heme iron in myoglobin and hemoglobin is in the ____________ oxidation state.
Page 9
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Chapter 8: Enzymes: Basic Concepts and Kinetics
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Q1) What term is used to describe the dynamic recognition of the substrate when binding to an enzyme occurs?
A) allosteric modulation
B) transition state enhancement
C) sequential binding
D) induced fit
E) None of the answers is correct.
Q2) How are the types of inhibition kinetically distinguishable?
Q3) What is the common strategy by which catalysis occurs?
A) increasing the probability of product formation
B) shifting the reaction equilibrium
C) stabilization of transition state
D) All of the answers are correct.
E) None of the answers is correct.
Q4) How do the intermediate steps in multisubstrate enzyme mechanisms differ?
Q5) Compounds that resemble the transition state of a catalyzed reaction and inhibit enzyme activity are called ____________________________.
Q6) How is the substrate bound to the active site?
Q7) What is the Michaelis-Menten equation? Define all parameters.
Page 10
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Chapter 9: Catalytic Strategies
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Q1) The mechanism of chymotrypsin involves the formation of an unstable __________________ -shaped intermediate that is stabilized by the oxyanion hole.
Q2) What is the common nucleophile found in cysteine,metallo-,and aspartyl proteases?
Q3) If you carried out site-directed mutagenesis of subtilisin,changing serine 221 to isoleucine,what would you expect?
A) a large change in K<sub>M</sub>
B) a small change in K<sub>M </sub>
C) a large change in k<sub>cat</sub>
D) a large change in K<sub>M</sub><sub> </sub>and a large change in k<sub>cat</sub>
E) a small change in K<sub>M</sub><sub> </sub>and <sub> </sub>a large change in k<sub>cat</sub>
Q4) What process converts chymotrypsinogen to chymotrypsin?
A) metal ion binding
B) peptide bond cleavage
C) coenzyme association
D) cysteine methylation
E) proline hydroxylation
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Chapter 10: Regulatory Strategies
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Sample Questions
Q1) Which of the following is an example of a zymogen?
A) pepsinogen
B) procarboxypeptidase
C) T-form of ACTase
D) All of the answers are correct.
E) pepsinogen and procarboxypeptidase
Q2) Changes in ATCase conformation were detected by crystallizing the enzyme in the presence of PALA (N-(phosphonacetyl)-L-aspartate).What is PALA?
A) a radioactive tag that binds to the subunits
B) a substrate analog that resembles the transition state
C) a fluorescent allosteric inhibitor analog
D) All of the answers are correct.
E) None of the answers is correct.
Q3) One type of hemophilia is due to A) vitamin K deficiency.
B) loss of the gene for prothrombin.
C) loss of the gene for antihemophilic factor.
D) All of the answers are correct.
E) None of the answers is correct.
Q4) What is the dual action of thrombin?
Page 12
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Chapter 11: Carbohydrates
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Q1) Which of the following explains how some viruses gain entry into specific cells?
A) by attaching to ion channels
B) by cleaving the glycosidic bonds of cell surface glycoproteins and altering protein shapes
C) by binding to glycoproteins on the cell surface that are unique to specific cells
D) All of the answers are correct.
E) None of the answers is correct.
Q2) Which of the following terms describes a class of compounds with the molecular formula (CH<sub>2</sub>O)<sub>n</sub>?
A) proteoglycans
B) glycogen
C) mucoproteins
D) polysaccharides
E) monosaccharides
Q3) A given protein with several potential glycosylation sites can have many different glycosylated structures called ________________.
Q4) How does a genetic mutation account for some of the different human blood types?
Q5) What is the advantage of having different blood types within a species?
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Chapter 12: Lipids and Cell Membranes
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Q1) Which of the following statements is consistent with the structure of biological membranes?
A) All membrane proteins are integral and associate with the hydrophobic region of the membrane.
B) Both proteins and lipids readily undergo transverse ("flip-flop") diffusion from the inside to the outside of the membrane.
C) Membranes are symmetric.
D) The membrane lipids self-assemble to form the lipid bilayer.
E) A biological membrane consists of proteins sandwiched between two layers of lipids, which are referred to as a lipid bilayer.
Q2) In animals,________________ is the key regulator of membrane fluidity.
Q3) What are the two systems for naming the positions of the double bonds? Provide examples.
Q4) The temperature at which a phospholipid membrane transitions from a rigid to a fluid state is referred to as _______________.
Q5) What are liposomes? What are some of the current commercial applications?
Q6) Membranes carry out what functions due to their electrically polarized structure?
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Page 14

Chapter 13: Membrane Channels and Pumps
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Q1) Ion channels
A) can be selective.
B) exist in open and closed states.
C) in the open state often spontaneously convert into an inactivated state.
D) can be selective and exist in open and closed states.
E) All of the answers are correct.
Q2) ABC transporters utilize ____________ to accomplish active transport.
Q3) Describe the functional domains of the sarcoplasmic reticulum Ca<sup>2+</sup> ATPase.
Q4) What is the general term for membrane transporters that couple uphill transport of one species to the downhill flow of another species?
A) cotransporters
B) antiporters
C) symporters
D) uniporters
E) None of the answers is correct.
Q5) What is the "ball-and-chain" model?
Q6) How does energy affect the functioning of the Na<sup>+</sup>-K<sup>+</sup> ATPase?
Q7) How does active transport differ from passive?
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Chapter 14: Signal-Transduction Pathways
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Q1) Advantages of second messengers include
A) the signal can be amplified by making many second messengers.
B) second messengers can freely diffuse to other sites within the cell.
C) a few common second messengers can be used in multiple signaling pathways.
D) All of the answers are correct.
E) A and C.
Q2) How does binding of epinephrine initiate cAMP production? Discuss briefly in terms of receptor structure and function.
Q3) What is the difference between heterotrimeric G proteins and small G proteins?
Q4) What is the relationship between monoclonal antibodies,breast cancer,and HER2?
Q5) The binding of IP<sub>3</sub> to the IP<sub>3</sub> receptor results in the release of __________ from the endoplasmic reticulum.
Q6) The catalytically active form of the insulin receptor is a result of phosphorylation of specific ____________ residues in the activation loop.
Q7) The ________ receptor is approximately 50% identical in amino acid sequence with the EGF receptor and has similar domain structure,but it does not bind any known ligand.
Q8) What happens when signaling paths are not terminated properly?
Q9) Draw the reaction catalyzed by tyrosine kinase (no mechanism necessary).
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Chapter 15: Metabolism: Basic Concepts and Design
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Q1) Metabolic pathways that require energy and are often biosynthetic processes are
A) anabolic.
B) catabolic.
C) allobolic.
D) All of the answers are correct
E) None of the answers is correct.
Q2) What type of organism uses energy from sunlight and converts it to chemical energy?
A) chemotrophs
B) phototrophs
C) heterotrophs
D) autotrophs
E) None of the answers is correct.
Q3) Which coenzymes contain adenosine phosphate units?
A) NADH
B) FADH2
C) coenzyme A
D) NADPH
E) All of the answers are correct.
Q4) What is the phosphorylation potential of a cell?
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Chapter 16: Glycolysis and Gluconeogenesis
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Q1) The formation of ATP is due to direct transfer of a phosphoryl group and is called
Q2) What two 3-carbon molecules are generated by the cleavage of fructose-1,6-bisphosphate?
A) glyceraldehyde-3-phosphate and 3-phosphoglycerate
B) glyceraldehyde-3-phosphate and dihydroxyacetone phosphate
C) pyruvate and phosphoenolpyruvate
D) enolase and 2-phosphoglycerate
E) glyceraldehyde-3-phosphate and pyruvate
Q3) What is the additional metabolite that is required for the conversion of 3-phosphoglycerate to 2-phosphoglycerate?
A) 1-phosphoglycerate
B) diacylglycerol
C) NADH
D) 2,3-bisphosphoglycerate
E) 1,3-bisphosphoglycerate
Q4) What astounding discovery was made by the Buchners?
Q5) What two functions are attributed to substrate cycles?
Q6) Glycolysis produces a net of ________ moles of ATP per 1 mole of glucose.
Page 18
Q7) The key enzyme that regulates the pace of glycolysis is

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Chapter 17: The Citric Acid Cycle
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Q1) Beri-beri is caused by a deficiency of __________________.
Q2) Which of the following enzymes are found in the glyoxylate cycle but not in the citric acid cycle?
A) malate synthase and isocitrate dehydrogenase
B) glyoxylate synthase and malate synthase
C) isocitrate lyase and malate dehydrogenase
D) malate synthase and isocitrate lyase
E) succinyl CoA synthetase and glyoxylate synthase
Q3) In addition to pyruvate dehydrogenase,which of the following enzymes is a key regulatory site in the citric acid cycle?
A) malate dehydrogenase
B) \(\alpha\)-ketoglutarate dehydrogenase
C) succinyl CoA synthetase
D) succinate dehydrogenase
E) None of the answers is correct.
Q4) The ?G??=-21 kJ mol<sup>-1</sup> for the reaction catalyzed by isocitrate dehydrogenase,yet the ?G?? = +29.7 kJ mol<sup>-1</sup> for the reaction catalyzed by malate dehydrogenase.Both of these reactions involve the oxidation of a secondary alcohol.Give an explanation as to why the oxidation of isocitrate is so exergonic.
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Chapter 18: Oxidative Phosphorylation
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Q1) When glucose is totally oxidized to CO<sub>2</sub> and H<sub>2</sub>O and the glycerol 3-phosphate shuttle is used,how many ATP molecules are made by oxidative phosphorylation (nonsubstrate-level phosphorylation)relative to the maximum yield?
A) 12 out of 30
B) 26 out of 30
C) 26 out of 32
D) 12 out of 32
E) None of the answers is correct.
Q2) The unequal distribution of H<sup>+</sup> across the inner mitochondrial membrane creates a ________________ force.
Q3) Acceptor control of oxidative phosphorylation means that the rate of respiration depends upon the level of __________.
Q4) Describe the major defensive strategy that cells employ to prevent the harmful effects of the reactive oxygen species (ROS)that are inevitably produced during respiration.
Q5) _________________ is a poison because it blocks the flow of electrons from cytochrome c to oxygen.
Q6) How does the glycerol 3-phosphate shuttle function?
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Chapter 19: The Light Reactions of Photosynthesis
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Q1) In bacterial photosynthesis,how would the light energy be used if the reduced bacteriopheophytin (BPh<sup>-</sup> returned the electron to the P960<sup>+</sup> cytochrome?
A) It would follow a separate electron-transport chain.
B) It would be lost as heat.
C) It would stimulate the ejection of a second electron.
D) A proton would be pumped.
E) None of the answers is correct.
Q2) The manganese center of photosystem II converts _________ to __________.
Q3) Electrons flow from photosystem II to photosystem I through the ________________ complex.
Q4) What is another name for the CF<sub>1</sub>-CF<sub>0</sub> complex?
A) ATP synthase
B) photosystem I
C) photosystem II
D) ferredoxin- NADP<sup>+</sup> reductase
E) cytochrome bf complex
Q5) Describe the process of cyclic photophosphorylation.
Q6) In _______________,ATP is generated without the concomitant formation of NADPH.
Q7) Write the overall reaction of photosystem II.
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Chapter 20: The Calvin Cycle and the Pentose Phosphate
Pathway
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Q1) What pathway ensures that sufficient amounts of CO<sub>2</sub> are available to minimize wasteful photorespiration by transporting CO<sub>2</sub> from the mesophyll cells to the bundle sheath cells?
A) crassulacean acid metabolism
B) gluconeogenesis
C) C<sub>4</sub><sub> </sub>pathway
D) sucrose synthesis
E) cellulose synthesis
Q2) The enzymes that catalyze the dark reactions of photosynthesis are located in the ___________ of the chloroplasts.
Q3) How many ATP are required by the C<sub>4</sub> pathway for each hexose that is produced?
A) 48
B) 30
C) 24
D) 18
E) 12
Q4) Why are components of the Calvin cycle called the "dark reactions"?
Q5) Describe the three stages of the Calvin cycle.
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Chapter 21: Glycogen Metabolism
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Q1) Why does liver possess a specific enzyme that can cleave glucose 6-phosphate to form glucose and orthophosphate?
Q2) What reaction cleaves a bond by the addition of orthophosphate?
A) phosphorolysis
B) phosphatase
C) transphosphorylation
D) oxidative phosphorylation
E) None of the answers is correct.
Q3) Phosphorylase kinase becomes fully active by being phosphorylated and binding
Q4) What type of glycosidic bond is found at the branch points of glycogen?
A) \(\alpha\)-1,2
B) \(\alpha\)-1,4
C) \(\alpha\)-1,6
D) \(\beta\)-1,4
E) \(\beta\)-1,6
Q5) What are the fates of the glucose-1-phosphate derived from glycogen?
Q6) By what mechanism is phosphorylase kinase activated by Ca<sup>2+</sup> levels of 1 M?
Q7) Why must glycogen control be manifested differently in muscle and liver?
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Chapter 22: Fatty Acid Metabolism
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Q1) Coenzyme(s)involved in the degradation of saturated fatty acyl CoA include(s)
A) FAD.
B) NAD<sup>+</sup>.
C) TPP.
D) FAD and NAD<sup>+</sup>.
E) All the answers are correct.
Q2) How are unsaturated fatty acids degraded?
Q3) The first step of \(\beta\) oxidation is a(n)_________-linked oxidation of the fatty acyl chain.
Q4) What are the similarities between fatty acid synthesis and degradation?
Q5) How is acetyl CoA carboxylase regulated globally?
A) By formation of inactive fibers
B) By the enzyme being switched off by phosphorylation and activated by dephosphorylation
C) By zymogen activation
D) By the binding of cAMP
E) None of the answers is correct.
Q6) \(\beta\) oxidation of odd-numbered fatty acids produces acetyl-CoA and _______________.
Q7) What is the fate of glycerol released during lipolysis?
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Chapter 23: Protein Turnover and Amino Acid Catabolism
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Q1) Describe how the urea cycle is linked to the citric acid cycle.
Q2) Ubiquitin-tagged proteins are digested by the __________________.
Q3) What enzyme catalyzes an oxidative deamination using either NAD<sup>+</sup> or NADP<sup>+</sup>?
A) glutamate dehydrogenase
B) \(\alpha\)-ketoglutarate dehydrogenase
C) glutamate deaminase
D) \(\alpha\)-ketoglutarate reductase
E) None of the answers is correct.
Q4) Four of the five enzymes in the urea cycle are evolutionarily related to enzymes found in
A) glucose transport.
B) electron transport chain.
C) nucleotide biosynthesis.
D) ubiquitination.
E) None of the answers is correct.
Q5) Why are four or more chains of ubiquitin particularly effective as a signal for degradation?
Q6) What are some types of enzyme-catalyzed reactions that require pyridoxal phosphate as a coenzyme?
Page 25
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Chapter 24: The Biosynthesis of Amino Acids
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Q1) In comparing transaminase enzymes,certain amino acids have been conserved.What are these amino acids,and how are they important in determining the proper chirality of the new amino acid?
Q2) Describe the structure and function of the FeMo cofactor.
Q3) The enzyme _______________ contains a selenium analogue of cysteine.
Q4) Which of the following is a versatile carrier of several different one-carbon units?
A) pyridoxal phosphate
B) biotin
C) tetrahydrofolate
D) coenzyme A
E) None of the answers is correct.
Q5) The ATP-binding region of the nitrogen-fixating reductase is a(n)___________ domain.
A) iron-sulfur
B) electron-binding
C) P-loop NTPase family
D) molybdenum-binding
E) All the answers are correct.
Q6) How does the herbicide glyphosate work?
Page 26
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Chapter 25: Nucleotide Biosynthesis
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Q1) Amination of _____ produces CTP.
A) TTP
B) ATP
C) UTP
D) GTP
E) OTP
Q2) _______________ disease is caused by a genetic mutation resulting in the absence of hypoxanthine-guanine phosphoribosyl transferase.
Q3) In the de novo synthesis of DNA and RNA,
A) ribonucleotides are made from deoxynucleotides.
B) deoxyribonucleotides are made from ribonucleotides.
C) dideoxyribonucleotides are the precursors for both.
D) ribonucleotides and deoxyribonucleotides are made by independent pathways.
E) None of the answers is correct.
Q4) What is the approximate rate change when the enzyme orotidylate decarboxylase decarboxylates orotidylate to form UMP?
Q5) Some individuals with a deficiency in the enzyme adenosine deaminase exhibit _______________ (bubble boy disease).
Q6) How is the reciprocal use of nucleotides useful in purine synthesis?
Page 27
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Chapter 26: Biosynthesis of Membrane Lipids and Steroids
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Q1) Hydroxylation of cholesterol by cytochrome P450 requires
A) NADPH.
B) O<sub>2</sub>
C) PLP.
D) thiamine.
E) NADPH and O<sub>2</sub>.
Q2) How do blood levels of lipoproteins serve diagnostic purposes?
Q3) How is methionine metabolism related to the synthesis of phosphatidyl choline?
Q4) Vitamin D<sub>3</sub> is converted into ______________________,which is an active hormone that functions as a transcription factor.
Q5) The starting materials necessary to synthesize sphingosine are
A) palmitoyl CoA and serine.
B) acetyl CoA and glycine.
C) palmitoyl CoA and aspartate.
D) acetyl CoA and glutamine.
E) None of the answers is correct.
Q6) ______________________ are sphingolipids that contain an oligosaccharide unit having at least one sialic acid residue.
Q7) What is the role of phosphatidyl choline in the synthesis of sphingomyelin?
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Chapter 27: The Integration of Metabolism
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Q1) What are the two hypotheses supporting low-carbohydrate-high-protein diets as an effective weight losing strategy?
Q2) ____________________ results when insulin is absent due to autoimmune destruction of the cells of the pancreas.
Q3) When levels of ketone bodies are high,the _________________ can no longer maintain acid-base balance in the blood.
Q4) ATP production from ___________________ is essential for long-distance running.
Q5) Glycolysis and gluconeogenesis are usually _________________ regulated.
Q6) In a typical human male,which of the following most closely approximates the energy content (in kcal)of triacylglycerols stored in adipose tissue?
A) 13,500 kcal
B) 135,000 kcal
C) 1,350,000 kcal
D) 13,500 cal
E) None of the answers is correct.
Q7) Describe the stages of ethanol consumption that affect liver damage and lead to death.
Q8) What are some of the primary metabolic fates of acetyl CoA in animals?
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Chapter 28: DNA Replication, repair, and Recombination
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Q1) DNA polymerase III is able to correct mistakes in replication due to its _________________ function.
Q2) Why is the site of DNA synthesis called the replication fork?
Q3) The tertiary structures in DNA are created by the process known as ______________.
Q4) What is a Klenow fragment?
Q5) UV light causes damage to DNA by forming __________________.
Q6) How is replication specificity dictated?
A) Proper base-pairing is dictated more by shape than by hydrogen bonding capacity.
B) Enzyme interactions with the DNA act as a "ruler" to determine if the properly spaced base pair has been formed.
C) The bond is broken and reformed to ensure its accurate placement at each base pair.
D) All the answers are correct.
E) A and B are both correct.
Q7) ________________ are intermediates in recombination pathways composed of four polynucleotide chains in a cross-like structure.
Q8) How is the processivity of DNA polymerase III accomplished?
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Chapter 29: RNA Synthesis and Processing
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Q1) What is a common feature of both protein-dependent and protein-independent termination signals in transcription?
Q2) 19.The enzyme _________________ transcribes a single precursor that encodes the 18S rRNA,the 28S rRNA,and the 5.8S rRNA.
Q3) Which of the following changes the nucleotide sequence of RNA after transcription occurs,by processes other than RNA splicing?
A) RNA editing
B) RNA proofing
C) RNA substitution
D) RNA mutation
E) None of the answers is correct.
Q4) Describe some of the significant differences between eukaryotic and prokaryotic transcription and translation.
Q5) Proteins that possess alternative splicing products include
A) calcitonin.
B) hemoglobin .
C) apolipoprotein.
D) calcitonin and apolipoprotein.
E) hemoglobin and apolipoprotein.
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Chapter 30: Protein Synthesis
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Q1) What term describes the RNA-directed process of protein synthesis?
A) transcription
B) translation
C) Merrifield synthesis
D) ribozyme-directed protein synthesis
E) None of the answers is correct.
Q2) Which of the following is (are)required for initiation of protein synthesis in bacteria?
A) mRNA
B) the 30S subunit
C) fmet-tRNA<sub>f</sub>
D) GTP
E) All of the answers are correct.
Q3) What role does the amino acid itself play in the accurate placement of the charged tRNA at the codon?
Q4) Proteins destined for extracellular release must first bind to the _________________ in the lumen of the ER.
Q5) What are the names for the tRNA binding sites on the ribosome?
Q6) How does puromycin inhibit protein synthesis?
Q7) The error frequency of protein synthesis is approximately _____________.
Page 32
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Chapter 31: The Control of Gene Expression in Prokaryotes
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Q1) Is it likely that the DNA binding sites for a repressor evolved from a common ancestor?
Q2) In which pathway is the viral genome incorporated into the bacterial DNA?
A) attenuation
B) lysogenic
C) lytic
D) trp operon
E) None of the answers is correct.
Q3) A chemical commonly used to induce the lac operon in laboratory experiments is A) lactose.
B) X-Gal.
C) IPTG.
D) galactose.
E) None of the answers is correct.
Q4) E.coli is the organism in which many _______________ mechanisms were first discovered.
Q5) A unit of gene expression that allows controlled and coordinated expression of a set of proteins is called a(n)__________________.
Q6) How does the lac repressor find its binding site on DNA?
Q7) How does the Cro protein promote the lytic state?
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Chapter 32: The Control of Gene Expression in Eukaryotes
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Q1) When a steroid hormone receptor binds its ligand,it induces a conformational change in the ligand-binding domain which allows the binding of a(n)_______________.
Q2) What is meant by combinatorial control of transcription in eukaryotes,and what is the advantage to this mechanism?
Q3) Give examples of epigenomic changes resulting in different cell types.
Q4) In eukaryotes,DNA-binding proteins bind to DNA by which of the following DNA-binding structures?
A) Cys<sub>2 </sub>His<sub>2</sub> zinc-finger domain
B) homeodomain
C) closed loops called lariats
D) Cys<sub>2 </sub>His<sub>2</sub> zinc-finger domain and homeodomain
E) Cys<sub>2 </sub>His<sub>2</sub> zinc-finger domain and closed loops called lariats
Q5) Describe the structure and function of the histone octamer.
Q6) Describe the arrangement of histones and associated DNA in a nucleosome.
Q7) The human genome contains genes for about _______________ proteins.
Q8) DNA regions that serve as binding sites for transcription factors which can act at a distance to perturb the local chromatin structure are called _________________.
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Chapter 33: Sensory Systems
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Q1) Mutant mice lacking the VR1 receptor are less responsive to the taste of capsaicin and can endure noxious levels of _______________.
Q2) Which of the following taste sensations is not detected by 7TM receptors?
A) umami (delicious)
B) sweet
C) salty
D) bitter
E) All of the answers are correct.
Q3) Which G-protein subunit is expressed in taste buds?
A) transducin
B) Rho
C) \(\alpha\)<sub>olf</sub>
D) gustducin
E) GNAL
Q4) What clues indicate that protein receptors are important in detection of smells?
Q5) Capsaicin is a chemical found in _______________.
Q6) In terms of sequence structure,OR family proteins are 20% identical to the ________________.
Q7) Salty tastes are detected through _________________.
Page 35
Q8) Describe the steps leading to the detection of light.
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Chapter 34: The Immune System
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Q1) What are the proteases released by cytotoxic T cells that initiate the apoptotic cascade in virus-infected cells?
A) caspases
B) cathepsins
C) granzymes
D) calpains
E) None of the answers is correct.
Q2) How is cyclosporin useful in medical therapy?
Q3) The approximate number of antibodies that humans can generate is
A) 10<sup>8</sup>.
B) 10<sup>12</sup>.
C) 10<sup>16</sup>.
D) 10<sup>20</sup>.
E) None of the answers is correct.
Q4) The immunoglobulin with the highest serum concentration is _______________.
Q5) Proteins necessary for binding and displaying portions of foreign proteins are encoded by the ____________________.
Q6) A(n)__________________ disease is one wherein the body attacks itself and produces self-antigens.
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Chapter 35: Molecular Motors
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Q1) Bacterial motors differ from eukaryotic ones in that the bacterial motor
A) moves along a polymeric track.
B) moves when ATP is hydrolyzed.
C) moves when GTP is hydrolyzed.
D) spins around a central axis.
E) None of the answers is correct.
Q2) Energy used to propel molecular motors includes
A) ATP.
B) ion gradients.
C) heat.
D) light.
E) ATP and ion gradients.
Q3) Describe the experiment that supports the proposed role of the lever arm in myosin motor activity.
Q4) Troponin reacts in response to the _______________ ion.
Q5) What is the "biased random walk" movement of bacteria,and when do they engage in this type of movement?
Q6) A helical section of myosin that moves dramatically when NTP is bound is called the
Q7) How does the action of kinesin differ from that of myosin on its track?
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Chapter 36: Drug Development
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Q1) Give an example of how a drug was discovered by a chance observation.
Q2) Thiopurines such as 6-thioguanine are used to treat immune disorders and leukemia.Some individuals who are treated show signs of toxicity at doses well tolerated by most patients.Explain the reason for this toxicity.
Q3) The most notable structural feature of penicillin is a four-membered ring referred to as a ______________ ring.
Q4) Which of the following enzymes is associated with the inflammatory response?
A) phosphodiesterase 5
B) HMG-CoA reductase
C) \(\beta\)-lactamase
D) cyclooxygenase 2
E) None of the answers is correct.
Q5) What term describes a molecule that binds to a target molecule?
A) substrate
B) effector
C) ligand
D) cosubstrate
E) None of the answers is correct.
Q6) The current cost of developing a new drug is ____________ .
Page 38
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